1lld: Difference between revisions

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-[[Image:1lld.gif|left|200px]]
-<!--
+==MOLECULAR BASIS OF ALLOSTERIC ACTIVATION OF BACTERIAL L-LACTATE DEHYDROGENASE==
-The line below this paragraph, containing "STRUCTURE_1lld", creates the "Structure Box" on the page.
+<StructureSection load='1lld' size='340' side='right'caption='[[1lld]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1lld]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bifidobacterium_longum_subsp._longum Bifidobacterium longum subsp. longum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LLD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LLD FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
-{{STRUCTURE_1lld|  PDB=1lld  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lld FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lld OCA], [https://pdbe.org/1lld PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lld RCSB], [https://www.ebi.ac.uk/pdbsum/1lld PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lld ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/LDH2_BIFL2 LDH2_BIFL2] Catalyzes the conversion of lactate to pyruvate.[HAMAP-Rule:MF_00488]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ll/1lld_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lld ConSurf].
+<div style="clear:both"></div>
-'''MOLECULAR BASIS OF ALLOSTERIC ACTIVATION OF BACTERIAL L-LACTATE DEHYDROGENASE'''
+==See Also==
+*[[Lactate dehydrogenase 3D structures|Lactate dehydrogenase 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-The three-dimensional structure of allosteric L-lactate dehydrogenase from Bifidobacterium longum, the first example of a T-state structure of L-lactate dehydrogenase, has been determined to 2.0 A. A comparative study of this structure with the previously reported R-state structure from Bacillus stearothermophilus has revealed the allosteric activation mechanism of the bacterial L-lactate dehydrogenase. The fructose 1,6-bisphosphate-induced conformational change at the effector site and the substrate affinity change at the activity site are clearly shown at a molecular level. Coupling of these changes can be simply explained by a set of concerted rotations between subunits in the tetramer of the enzyme. This T to R transition is the first example for a tetrameric allosteric protein where the rotations occur around each of three axes of symmetry.
+[[Category: Bifidobacterium longum subsp. longum]]
+[[Category: Large Structures]]
-==About this Structure==
+[[Category: Iwata S]]
-LLD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bifidobacterium_longum_bv._longum Bifidobacterium longum bv. longum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LLD OCA].
+[[Category: Ohta T]]
-==Reference==
-Molecular basis of allosteric activation of bacterial L-lactate dehydrogenase., Iwata S, Ohta T, J Mol Biol. 1993 Mar 5;230(1):21-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8450537 8450537]
-[[Category: Bifidobacterium longum bv. longum]]
-[[Category: L-lactate dehydrogenase]]
-[[Category: Single protein]]
-[[Category: Iwata, S.]]
-[[Category: Ohta, T.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 00:02:09 2008''